Thymidylate synthase
From Proteopedia
(Difference between revisions)
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**[[1nce]] - EcTS (mutant) + inhibitor+ UMP<BR /> | **[[1nce]] - EcTS (mutant) + inhibitor+ UMP<BR /> | ||
**[[1ddu]], [[1tdu]] - EcTS + deoxyuridine derivative + inhibitor<br /> | **[[1ddu]], [[1tdu]] - EcTS + deoxyuridine derivative + inhibitor<br /> | ||
| + | **[[6cdz]] - EcTS + deoxyuridine + UMP<br /> | ||
**[[4gev]] - EcTS + deoxyuridine derivative + cofactor analog<br /> | **[[4gev]] - EcTS + deoxyuridine derivative + cofactor analog<br /> | ||
**[[4knz]] - EcTS + deoxyuridine derivative + folate derivative<br /> | **[[4knz]] - EcTS + deoxyuridine derivative + folate derivative<br /> | ||
Revision as of 22:06, 25 September 2018
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3D structures of thymidylate synthase
Updated on 25-September-2018
References
- ↑ Kaneda S, Nalbantoglu J, Takeishi K, Shimizu K, Gotoh O, Seno T, Ayusawa D. Structural and functional analysis of the human thymidylate synthase gene. J Biol Chem. 1990 Nov 25;265(33):20277-84. PMID:2243092
- ↑ Rahman L, Voeller D, Rahman M, Lipkowitz S, Allegra C, Barrett JC, Kaye FJ, Zajac-Kaye M. Thymidylate synthase as an oncogene: a novel role for an essential DNA synthesis enzyme. Cancer Cell. 2004 Apr;5(4):341-51. PMID:15093541
- ↑ Finer-Moore JS, Fauman EB, Morse RJ, Santi DV, Stroud RM. Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase. Protein Eng. 1996 Jan;9(1):69-75. PMID:9053905
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